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Database: UniProt
Entry: A0A3Q2DYF9_CYPVA
LinkDB: A0A3Q2DYF9_CYPVA
Original site: A0A3Q2DYF9_CYPVA 
ID   A0A3Q2DYF9_CYPVA        Unreviewed;       195 AA.
AC   A0A3Q2DYF9;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Rho GDP-dissociation inhibitor 1 {ECO:0000256|ARBA:ARBA00040620};
DE   AltName: Full=Rho-GDI alpha {ECO:0000256|ARBA:ARBA00041559};
GN   Name=ARHGDIA {ECO:0000313|Ensembl:ENSCVAP00000023994.1};
OS   Cyprinodon variegatus (Sheepshead minnow).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC   Cyprinodon.
OX   NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000023994.1, ECO:0000313|Proteomes:UP000265020};
RN   [1] {ECO:0000313|Ensembl:ENSCVAP00000023994.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Controls Rho proteins homeostasis. Regulates the GDP/GTP
CC       exchange reaction of the Rho proteins by inhibiting the dissociation of
CC       GDP from them, and the subsequent binding of GTP to them. Retains Rho
CC       proteins such as CDC42, RAC1 and RHOA in an inactive cytosolic pool,
CC       regulating their stability and protecting them from degradation.
CC       Actively involved in the recycling and distribution of activated Rho
CC       GTPases in the cell, mediates extraction from membranes of both
CC       inactive and activated molecules due its exceptionally high affinity
CC       for prenylated forms. Through the modulation of Rho proteins, may play
CC       a role in cell motility regulation. In glioma cells, inhibits cell
CC       migration and invasion by mediating the signals of SEMA5A and PLXNB3
CC       that lead to inactivation of RAC1. {ECO:0000256|ARBA:ARBA00037489}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the Rho GDI family.
CC       {ECO:0000256|ARBA:ARBA00009758}.
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DR   AlphaFoldDB; A0A3Q2DYF9; -.
DR   Ensembl; ENSCVAT00000005327.1; ENSCVAP00000023994.1; ENSCVAG00000007775.1.
DR   GeneTree; ENSGT00390000006233; -.
DR   OMA; EYEFFTT; -.
DR   Proteomes; UP000265020; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005094; F:Rho GDP-dissociation inhibitor activity; IEA:InterPro.
DR   GO; GO:0007266; P:Rho protein signal transduction; IEA:InterPro.
DR   Gene3D; 2.70.50.30; Coagulation Factor XIII, subunit A, domain 1; 1.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR000406; Rho_GDI.
DR   InterPro; IPR024792; RhoGDI_dom_sf.
DR   PANTHER; PTHR10980; RHO GDP-DISSOCIATION INHIBITOR; 1.
DR   PANTHER; PTHR10980:SF9; RHO GDP-DISSOCIATION INHIBITOR 1; 1.
DR   Pfam; PF02115; Rho_GDI; 1.
DR   PRINTS; PR00492; RHOGDI.
DR   SUPFAM; SSF81296; E set domains; 1.
PE   3: Inferred from homology;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265020}.
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   195 AA;  22305 MW;  15F5B6C40795A18D CRC64;
     MADNDAETEN EEPEPVNYKP PAQKSVKEIQ ELDKDDESLR KYKEALLGPG ITESDPNAPN
     VQVTRMALVC ETAPNPLVLD LQGDLEAFKK QAFVLKEGVE YKIKISFKVN KEIVSGLKYV
     QQTFRKGMKI DKSDYMVGSY GPRPTEYDFL TTIEEAPKGM LARGNYVIKS KFTDDDKHDH
     LSWEWNLNIK KDWND
//
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